BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 15528

Title: Solution structure of the protease-resistent domain of Xenopus ePABP2   PubMed: 18824697

Authors: Song, J.; Markley, J.

Citation: Song, Jikui; McGivern, Jered; Nichols, Karl; Markley, John; Sheets, Michael. "Structural basis for RNA recognition by a type II poly(A)-binding protein"  Proc. Natl. Acad. Sci. U.S.A. 105, 15317-15322 (2008).

Assembly members:
ePABP2-trp, polymer, 124 residues, Formula weight is not available

Natural source:   Common Name: African clawed frog   Taxonomy ID: 8355   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Xenopus Laevis

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
ePABP2-trp: AIAPCMQTTHSKMTAGAYTE GPPQPLSAEEKKEIDKRSVY VGNVDYGSTAQDLEAHFSSC GSINRITILCDKFSGHPKGY AYIEFAERNSVDAAVAMDET VFRGRTIKVLPKRTNMPGIS STDR

Data sets:
Data typeCount
13C chemical shifts460
15N chemical shifts124
1H chemical shifts715

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1protease-resistent domain, chain 11
2protease-resistent domain, chain 21

Entities:

Entity 1, protease-resistent domain, chain 1 124 residues - Formula weight is not available

1   ALAILEALAPROCYSMETGLNTHRTHRHIS
2   SERLYSMETTHRALAGLYALATYRTHRGLU
3   GLYPROPROGLNPROLEUSERALAGLUGLU
4   LYSLYSGLUILEASPLYSARGSERVALTYR
5   VALGLYASNVALASPTYRGLYSERTHRALA
6   GLNASPLEUGLUALAHISPHESERSERCYS
7   GLYSERILEASNARGILETHRILELEUCYS
8   ASPLYSPHESERGLYHISPROLYSGLYTYR
9   ALATYRILEGLUPHEALAGLUARGASNSER
10   VALASPALAALAVALALAMETASPGLUTHR
11   VALPHEARGGLYARGTHRILELYSVALLEU
12   PROLYSARGTHRASNMETPROGLYILESER
13   SERTHRASPARG

Samples:

sample_1: ePABP2-trp, [U-100% 13C; U-100% 15N], 1 mM; NaCl 100 mM; NaAc 10 mM

sample_2: ePABP2-trp, [U-100% 13C; U-100% 15N], 0.5 mM; ePABP2-trp 0.5 mM; NaCl 100 mM; NaAc 10 mM

sample_3: ePABP2-trp, [U-100% 15N], 0.5 mM; PEG 5%; NaCl 100 mM; NaAc 10 mM

sample_conditions_1: ionic strength: 100 mM; pH: 5.0; pressure: 1 atm; temperature: 308 K

sample_conditions_2: ionic strength: 100 mM; pH: 5.0; pressure: 1 atm; temperature: 302 K

Experiments:

NameSampleSample stateSample conditions
1H,15N-HSQCsample_1isotropicsample_conditions_1
1H,13C-HSQCsample_1isotropicsample_conditions_1
HNCACBsample_1isotropicsample_conditions_1
HCCONHsample_1isotropicsample_conditions_1
CBCACONHsample_1isotropicsample_conditions_1
CCONHsample_1isotropicsample_conditions_1
HCCHTOCSYsample_1isotropicsample_conditions_1
HBACONHsample_1isotropicsample_conditions_1
13C-EDITED 1H,1H-NOESY (aliph)sample_1isotropicsample_conditions_1
15N-EDITED 1H,1H-NOESYsample_1isotropicsample_conditions_1
13C,15N filtered, 13C EDITED 1H,1H-NOESYsample_2isotropicsample_conditions_1
15N IPAP HSQCsample_3anisotropicsample_conditions_2
13C-EDITED 1H,1H-NOESY (arom)sample_1isotropicsample_conditions_1

Software:

X-PLOR NIH v2.17.0, SCHWIETERS,C.D.,KUSZEWSKI,J.J.,TJANDRA,N.,CLORE,G.M. - refinement

xwinnmr v3.5, Bruker - collection

NMRPipe v97.027.12.56, Delagio,F. et al. - processing

SPARKY v3.113, Goddard,T.D. and Kneller,D.G. - data analysis

GARANT v2.1, Bartels,C. et al - data analysis

CYANA v2.1, Guntert,P. et al - structural calculation

NMR spectrometers:

  • Bruker DMX 750 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 900 MHz

Related Database Links:

PDB
GB AAI70309 AAI70311 AAR26263
REF NP_001084418
SP Q6TY21